2HDN
Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU |
| Temperature [K] | 298 |
| Detector technology | AREA DETECTOR |
| Detector | SDMS |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.710, 156.060, 134.830 |
| Unit cell angles | 90.00, 95.38, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.800 |
| Rwork | 0.180 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | an unrefined 2.7 Angstrom model of E. coli trypsin-modified EF-Tu-MgGDP consisting of residues 9 to 40 50 to 258 and 260 to 393 plus one Mg ion and GDP |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.820 |
| Phasing software | MERLOT |
| Refinement software | CNS |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 47.300 |
| High resolution limit [Å] | 2.700 |
| Rmerge | 0.099 |
| Number of reflections | 73085 |
| Completeness [%] | 92.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP |






